PMID- 10383425
OWN - NLM
STAT- MEDLINE
DCOM- 19990727
LR  - 20210209
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 27
DP  - 1999 Jul 2
TI  - Molecular cloning and characterization of MT-ACT48, a novel mitochondrial
      acyl-CoA thioesterase.
PG  - 19188-94
AB  - While characterizing Eps15 partners, we identified a 48-kDa polypeptide (p48)
      which was precipitated by Eps15-derived glutathione S-transferase fusion
      proteins. A search in a murine expressed sequence tag data base with N-terminal
      microsequences of p48 led to the identification of two complete cDNA clones
      encoding two isoforms of a 439-amino acid protein sharing 95% nucleic and amino
      acid identity. Northern blot and immunoblotting studies showed that p48 was
      ubiquitously expressed. A significant homology (19% identity and 40% similarity) 
      between p48 and rat brain cytosolic acyl-CoA thioesterase was observed in an
      80-amino acid C-terminal domain, retrieved from proteins from human, nematode,
      and plants. The thioesterase function of p48 was further demonstrated against
      long chain acyl-CoAs in a spectrophotometric assay. Furthermore, data obtained
      from sequence analysis showed that p48 contained a mitochondrial targeting
      signal, cleaved in mature protein as assessed by microsequencing. The
      mitochondrial localization of both endogenous and transfected p48 was confirmed
      by confocal microscopy. These results indicate that p48, called MT-ACT48
      (mitochondrial acyl-CoA thioesterase of 48 kDa), defines a novel family of
      mitochondrial long chain acyl-CoA thioesterases.
FAU - Poupon, V
AU  - Poupon V
AD  - CJF 97-10 INSERM, Faculte Necker-Enfants Malades, 156 rue de Vaugirard, 75756
      Paris Cedex 15, France.
FAU - Begue, B
AU  - Begue B
FAU - Gagnon, J
AU  - Gagnon J
FAU - Dautry-Varsat, A
AU  - Dautry-Varsat A
FAU - Cerf-Bensussan, N
AU  - Cerf-Bensussan N
FAU - Benmerah, A
AU  - Benmerah A
LA  - eng
SI  - GENBANK/AJ238893
SI  - GENBANK/AJ238894
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - EC 3.1.2.2 (Palmitoyl-CoA Hydrolase)
SB  - IM
MH  - 3T3 Cells
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Brain/enzymology
MH  - Cell Line
MH  - Cloning, Molecular
MH  - Cytosol/enzymology
MH  - Humans
MH  - Mice
MH  - Mitochondria/*enzymology
MH  - Molecular Sequence Data
MH  - Molecular Weight
MH  - Palmitoyl-CoA Hydrolase/*genetics/metabolism
MH  - Rabbits
MH  - Rats
MH  - Substrate Specificity
MH  - Transfection
EDAT- 1999/06/26 00:00
MHDA- 1999/06/26 00:01
CRDT- 1999/06/26 00:00
PHST- 1999/06/26 00:00 [pubmed]
PHST- 1999/06/26 00:01 [medline]
PHST- 1999/06/26 00:00 [entrez]
AID - 10.1074/jbc.274.27.19188 [doi]
AID - S0021-9258(19)74137-4 [pii]
PST - ppublish
SO  - J Biol Chem. 1999 Jul 2;274(27):19188-94. doi: 10.1074/jbc.274.27.19188.